Rat liver mitochondrial permeability transition: molecular mechanisms & dependencies

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

Human evidence only

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

Mangiferin exposure increased susceptibility to calcium-induced mitochondrial permeability transition.
Mangiferin → Rat liver mitochondrial permeability transition source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/mangiferin-research/15979560.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3de89f65f9561fd94c5f07121e8150f116c59277658d7e611a399dc2d963ec1f", "start_char": 0, "end_char": 2234, "text_sha256": "3de89f65f9561fd94c5f07121e8150f116c59277658d7e611a399dc2d963ec1f"}
experimental_model
Rat pretreatment and isolated mitochondrial calcium challenge
exposure
40 mg/kg mangiferin pretreatment; isolated mitochondria exposed to calcium
limitations
Mitochondrial challenge does not establish harm from usual oral intake; proposed quinone-thiol adduct mechanism was not fully proven.
nutrient_topic
Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
organism
Rattus norvegicus
plain_language
Lower oxidative readouts do not necessarily mean preserved membrane function.
primary_references
[mangiferin-p15979560] Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition. (2005). https://pubmed.ncbi.nlm.nih.gov/15979560/ DOI: 10.1016/j.abb.2005.05.015
tissue_or_cell_type
Liver mitochondria
Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 705–716
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat pretreatment and isolated mitochondrial calcium challenge · source_derived_draft · unverified_draft
### mangiferin-calcium-mpt Mangiferin exposure increased susceptibility to calcium-induced mitochondrial permeability transition. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Lower oxidative readouts do not necessarily mean preserved membrane function. organism: Rattus norvegicus tissue_or_cell_type: Liver mitochondria experimental_model: Rat pretreatment and isolated mitochondrial calcium challenge limitations: Mitochondrial challenge does not establish harm from usual oral intake; proposed quinone-thiol adduct mechanism was not fully proven. exposure: 40 mg/kg mangiferin pretreatment; isolated mitochondria exposed to calcium evidence_span: {"source_cache": "artifacts/mangiferin-research/15979560.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3de89f65f9561fd94c5f07121e8150f116c59277658d7e611a399dc2d963ec1f", "start_char": 0, "end_char": 2234, "text_sha256": "3de89f65f9561fd94c5f07121e8150f116c59277658d7e611a399dc2d963ec1f"} [mangiferin-p15979560] Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition. (2005). https://pubmed.ncbi.nlm.nih.gov/15979560/ DOI: 10.1016/j.abb.2005.05.015
Complete structured claim and evidence
The ferric complex did not elicit permeability transition and protected against its induction in the assay.
Mangiferin-ferric iron complex, assay-defined → Rat liver mitochondrial permeability transition source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"}
experimental_model
Iron-coordination spectroscopy and mitochondrial challenge
exposure
Assay-defined ferric iron-mangiferin complex
limitations
Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation.
nutrient_topic
Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
organism
Rattus norvegicus and cell-free chemistry
plain_language
Changing chemical form changed the membrane response.
primary_references
[mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
tissue_or_cell_type
Isolated mitochondria
Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 744–755
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Iron-coordination spectroscopy and mitochondrial challenge · source_derived_draft · unverified_draft
### mangiferin-complex-mpt The ferric complex did not elicit permeability transition and protected against its induction in the assay. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing chemical form changed the membrane response. organism: Rattus norvegicus and cell-free chemistry tissue_or_cell_type: Isolated mitochondria experimental_model: Iron-coordination spectroscopy and mitochondrial challenge limitations: Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation. exposure: Assay-defined ferric iron-mangiferin complex evidence_span: {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"} [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
Complete structured claim and evidence

The events it takes part in

A mechanism often involves more than two components. These are the full events, with every participant and its role.

Situations it appears in

Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

Open hypotheses

Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.

This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

Rat liver mitochondrial permeability transition